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- W2056594293 abstract "The first step in the activation of the classical pathway of complement cascade by immune complexes involves the binding of the C-terminal globular head regions of C1q to the Fc regions of IgG or IgM, each globular head being composed of the C-terminal halves of one A-, one B- and one C-chain. Recent studies using recombinant forms of globular region appear to suggest that each globular head of C1q may be composed of three, structurally and functionally, independent domains/modules. The heterotrimeric organisation thus could offer functional flexibility and versatility to the whole C1q molecule. The crystal structure of an adipocyte-specific serum protein, Acrp-30, has revealed the existence of a structural fold shared by members of a new C1q/tumor necrosis factor (TNF) superfamily, characterized by a distinctive globular domain. The protein members seem to be active as self-assembling noncovalent trimers, whose individual chains fold as compact ‘jellyroll' b sandwiches. The recognition of a C1q/TNF superfamily, which has wide-ranging functions, highlights the possibility that the globular regions of C1q may fulfill more binding functions than previously envisaged." @default.
- W2056594293 created "2016-06-24" @default.
- W2056594293 creator A5062104862 @default.
- W2056594293 date "2002-01-01" @default.
- W2056594293 modified "2023-10-12" @default.
- W2056594293 title "Recent Progress in the Understanding of the Structure- Function Relationships of the Globular Head Regions of C1q" @default.
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- W2056594293 doi "https://doi.org/10.1078/0171-2985-00138" @default.
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